Apical sorting by galectin-3-dependent glycoprotein clustering
(2007) In Traffic: the International Journal of Intracellular Transport 8(4). p.379-388- Abstract
- Epithelial cells are characterized by their polarized organization based on an apical membrane that is separated from the basolateral membrane domain by tight junctions. Maintenance of this morphology is guaranteed by highly specific sorting machinery that separates lipids and proteins into different carrier populations for the apical or basolateral cell surface. Lipid-raft-independent apical carrier vesicles harbour the beta-galactoside-binding lectin galectin-3, which interacts directly with apical cargo in a glycan-dependent manner. These glycoproteins are mistargeted to the basolateral membrane in galectin-3-depleted cells, dedicating a central role to this lectin in raft-independent sorting as apical receptor. Here, we demonstrate... (More)
- Epithelial cells are characterized by their polarized organization based on an apical membrane that is separated from the basolateral membrane domain by tight junctions. Maintenance of this morphology is guaranteed by highly specific sorting machinery that separates lipids and proteins into different carrier populations for the apical or basolateral cell surface. Lipid-raft-independent apical carrier vesicles harbour the beta-galactoside-binding lectin galectin-3, which interacts directly with apical cargo in a glycan-dependent manner. These glycoproteins are mistargeted to the basolateral membrane in galectin-3-depleted cells, dedicating a central role to this lectin in raft-independent sorting as apical receptor. Here, we demonstrate that high-molecular-weight clusters are exclusively formed in the presence of galectin-3. Their stability is sensitive to increased carbohydrate concentrations, and cluster formation as well as apical sorting are perturbed in glycosylation-deficient Madin-Darby canine kidney (MDCK) II cells. Together, our data suggest that glycoprotein cross-linking by galectin-3 is required for apical sorting of non-raft-associated cargo. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/671885
- author
- Delacour, Delphine ; Greb, Christoph ; Koch, Annett ; Salomonsson, Emma LU ; Leffler, Hakon LU ; Le Bivic, Andre and Jacob, Ralf
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- polarized cells, glycoprotein sorting, apical transport, galectin
- in
- Traffic: the International Journal of Intracellular Transport
- volume
- 8
- issue
- 4
- pages
- 379 - 388
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000244945200007
- scopus:33947214012
- ISSN
- 1398-9219
- DOI
- 10.1111/j.1600-0854.2007.00539.x
- language
- English
- LU publication?
- yes
- id
- 3808f5b8-2efd-46ee-a767-b3861ee35a20 (old id 671885)
- date added to LUP
- 2016-04-01 12:06:34
- date last changed
- 2022-04-13 06:16:14
@article{3808f5b8-2efd-46ee-a767-b3861ee35a20,
abstract = {{Epithelial cells are characterized by their polarized organization based on an apical membrane that is separated from the basolateral membrane domain by tight junctions. Maintenance of this morphology is guaranteed by highly specific sorting machinery that separates lipids and proteins into different carrier populations for the apical or basolateral cell surface. Lipid-raft-independent apical carrier vesicles harbour the beta-galactoside-binding lectin galectin-3, which interacts directly with apical cargo in a glycan-dependent manner. These glycoproteins are mistargeted to the basolateral membrane in galectin-3-depleted cells, dedicating a central role to this lectin in raft-independent sorting as apical receptor. Here, we demonstrate that high-molecular-weight clusters are exclusively formed in the presence of galectin-3. Their stability is sensitive to increased carbohydrate concentrations, and cluster formation as well as apical sorting are perturbed in glycosylation-deficient Madin-Darby canine kidney (MDCK) II cells. Together, our data suggest that glycoprotein cross-linking by galectin-3 is required for apical sorting of non-raft-associated cargo.}},
author = {{Delacour, Delphine and Greb, Christoph and Koch, Annett and Salomonsson, Emma and Leffler, Hakon and Le Bivic, Andre and Jacob, Ralf}},
issn = {{1398-9219}},
keywords = {{polarized cells; glycoprotein sorting; apical transport; galectin}},
language = {{eng}},
number = {{4}},
pages = {{379--388}},
publisher = {{Wiley-Blackwell}},
series = {{Traffic: the International Journal of Intracellular Transport}},
title = {{Apical sorting by galectin-3-dependent glycoprotein clustering}},
url = {{http://dx.doi.org/10.1111/j.1600-0854.2007.00539.x}},
doi = {{10.1111/j.1600-0854.2007.00539.x}},
volume = {{8}},
year = {{2007}},
}